메뉴 건너뛰기




Volumn 178, Issue 11, 1996, Pages 3044-3048

Dihydrolipoamide dehydrogenase from the halophilic archaeon Haloferax volcanii: Homologous overexpression of the cloned gene

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE;

EID: 0029903278     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.11.3044-3048.1996     Document Type: Article
Times cited : (42)

References (31)
  • 2
    • 0027272686 scopus 로고
    • High expression in Escherichia coli of the gene coding for dihydrofolate reductase of the extremely halophilic archaebacterium Haloferax volcanii
    • Blecher, O., S. Goldman, and M. Mevarech. 1993. High expression in Escherichia coli of the gene coding for dihydrofolate reductase of the extremely halophilic archaebacterium Haloferax volcanii. Eur. J. Biochem. 216:199-203.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 199-203
    • Blecher, O.1    Goldman, S.2    Mevarech, M.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0024530633 scopus 로고
    • Gene structure, organization and expression in archaebacteria
    • Brown, J. W., C. J. Daniels, and J. N. Reeve. 1989. Gene structure, organization and expression in archaebacteria. Crit. Rev. Microbiol. 16:287-338.
    • (1989) Crit. Rev. Microbiol. , vol.16 , pp. 287-338
    • Brown, J.W.1    Daniels, C.J.2    Reeve, J.N.3
  • 5
    • 0027195301 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of the gene encoding malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui
    • Cendrin, F., J. Chroboczek, G. Zaccai, H. Eisenberg, and M. Mevarech. 1993. Cloning, sequencing and expression in Escherichia coli of the gene encoding malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32:4308-4313.
    • (1993) Biochemistry , vol.32 , pp. 4308-4313
    • Cendrin, F.1    Chroboczek, J.2    Zaccai, G.3    Eisenberg, H.4    Mevarech, M.5
  • 6
    • 0023517503 scopus 로고
    • Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium
    • Charlebois, R. L., W. L. Lam, S. W. Cline, and W. F. Doolittle. 1987. Characterization of pHV2 from Halobacterium volcanii and its use in demonstrating transformation of an archaebacterium. Proc. Natl. Acad. Sci. USA 84:8530-8534.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8530-8534
    • Charlebois, R.L.1    Lam, W.L.2    Cline, S.W.3    Doolittle, W.F.4
  • 8
    • 0023926193 scopus 로고
    • Dihydrolipoamide dehydrogenase: A "new" function for an old enzyme?
    • Danson, M. J. 1988. Dihydrolipoamide dehydrogenase: a "new" function for an old enzyme? Biochem. Soc. Trans. 16:87-89.
    • (1988) Biochem. Soc. Trans. , vol.16 , pp. 87-89
    • Danson, M.J.1
  • 9
    • 8844250928 scopus 로고
    • Central metabolism of the Archaea
    • Danson, M. J. 1993. Central metabolism of the Archaea. New Compr. Biochem. 26:1-24.
    • (1993) New Compr. Biochem. , vol.26 , pp. 1-24
    • Danson, M.J.1
  • 10
    • 0023183181 scopus 로고
    • Dihydrolipoamide dehydrogenase from Trypanosoma brucei: Characterisation and cellular location
    • Danson, M. J., K. Conroy, A. McQuattie, and K. J. Stevenson. 1987. Dihydrolipoamide dehydrogenase from Trypanosoma brucei: characterisation and cellular location. Biochem. J. 243:661-666.
    • (1987) Biochem. J. , vol.243 , pp. 661-666
    • Danson, M.J.1    Conroy, K.2    McQuattie, A.3    Stevenson, K.J.4
  • 12
    • 0345136459 scopus 로고
    • Lipoic acid and dihydrolipoamide dehydrogenase in halophilic archaebacteria
    • Danson, M. J., D. W. Hough, N. Vettakkorumakankav, and K. J. Stevenson. 1991. Lipoic acid and dihydrolipoamide dehydrogenase in halophilic archaebacteria. NATO-ASI Ser. A 201:121-128.
    • (1991) NATO-ASI Ser. A , vol.201 , pp. 121-128
    • Danson, M.J.1    Hough, D.W.2    Vettakkorumakankav, N.3    Stevenson, K.J.4
  • 13
    • 0025099311 scopus 로고
    • A plasmid vector with a selectable marker for halophilic archaebacteria
    • Holmes, M. L., and M. L. Dyall-Smith. 1990. A plasmid vector with a selectable marker for halophilic archaebacteria. J. Bacteriol. 172:756-761.
    • (1990) J. Bacteriol. , vol.172 , pp. 756-761
    • Holmes, M.L.1    Dyall-Smith, M.L.2
  • 14
    • 0025738011 scopus 로고
    • Construction and use of halobacterial shuttle vectors and further studies on Haloferax DNA gyrase
    • Holmes, M. L., S. D. Nuttall, and M. L. Dyall-Smith. 1991. Construction and use of halobacterial shuttle vectors and further studies on Haloferax DNA gyrase. J. Bacteriol. 173:3807-3813.
    • (1991) J. Bacteriol. , vol.173 , pp. 3807-3813
    • Holmes, M.L.1    Nuttall, S.D.2    Dyall-Smith, M.L.3
  • 15
    • 0027968264 scopus 로고
    • Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid
    • Holmes, M., F. Pfeifer, and M. L. Dyall-Smith. 1994. Improved shuttle vectors for Haloferax volcanii including a dual-resistance plasmid. Gene 146:117-121.
    • (1994) Gene , vol.146 , pp. 117-121
    • Holmes, M.1    Pfeifer, F.2    Dyall-Smith, M.L.3
  • 16
    • 0020490794 scopus 로고
    • The mitochondrial glycine cleavage system
    • Kikuchi, G., and K. Hiraga. 1982. The mitochondrial glycine cleavage system. Mol. Cell. Biochem. 45:137-149.
    • (1982) Mol. Cell. Biochem. , vol.45 , pp. 137-149
    • Kikuchi, G.1    Hiraga, K.2
  • 17
    • 0021071824 scopus 로고
    • A general method for polyethylene-glycol-induced genetic transformation of bacteria and yeast
    • Klebe, R. J., J. V. Harriss, Z. D. Sharp, and M. G. Douglas. 1983. A general method for polyethylene-glycol-induced genetic transformation of bacteria and yeast. Gene 25:333-341.
    • (1983) Gene , vol.25 , pp. 333-341
    • Klebe, R.J.1    Harriss, J.V.2    Sharp, Z.D.3    Douglas, M.G.4
  • 18
    • 0024706289 scopus 로고
    • Shuttle vectors for the archaebacterium Halobacterium volcanii
    • Lam, W. L., and W. F. Doolittle. 1989. Shuttle vectors for the archaebacterium Halobacterium volcanii. Proc. Natl. Acad. Sci. USA 86:5478-5482.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5478-5482
    • Lam, W.L.1    Doolittle, W.F.2
  • 20
    • 0026079562 scopus 로고
    • Domains, motifs and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perham, R. N. 1991. Domains, motifs and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 30:8501-8512.
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 21
    • 0026576267 scopus 로고
    • Improved purification, crystallisation and primary structure of pyruvate-ferredoxin oxidoreductase from Halobacterium halobium
    • Plaga, W., F. Lottspeich, and D. Oesterhelt. 1992. Improved purification, crystallisation and primary structure of pyruvate-ferredoxin oxidoreductase from Halobacterium halobium. Eur. J. Biochem. 205:391-397.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 391-397
    • Plaga, W.1    Lottspeich, F.2    Oesterhelt, D.3
  • 22
    • 0001752523 scopus 로고
    • Studies on the nature and reaction of protein-bound lipoic acid
    • Reed, L. J., M. Koike, M. E. Levitch, and F. R. Leach. 1958. Studies on the nature and reaction of protein-bound lipoic acid. J. Biol. Chem. 232:143-158.
    • (1958) J. Biol. Chem. , vol.232 , pp. 143-158
    • Reed, L.J.1    Koike, M.2    Levitch, M.E.3    Leach, F.R.4
  • 23
    • 0024408596 scopus 로고
    • Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli
    • Richarme, G. 1989. Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli. J. Bacteriol. 171:6580-6585.
    • (1989) J. Bacteriol. , vol.171 , pp. 6580-6585
    • Richarme, G.1
  • 24
    • 0023049516 scopus 로고
    • Galactose and maltose stimulated lipoamide dehydrogenase activities related to the binding-protein dependent transport of galactose and maltose in toluenised cells of Escherichia coli
    • Richarme, G., and H. G. Heine. 1986. Galactose and maltose stimulated lipoamide dehydrogenase activities related to the binding-protein dependent transport of galactose and maltose in toluenised cells of Escherichia coli. Eur. J. Biochem. 156:399-405.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 399-405
    • Richarme, G.1    Heine, H.G.2
  • 26
    • 0011215428 scopus 로고
    • Dihydrolipoamide dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
    • Smith, L. D., S. Bungard, M. J. Danson, and D. W. Hough. 1987. Dihydrolipoamide dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem. Soc. Trans. 15:1097.
    • (1987) Biochem. Soc. Trans. , vol.15 , pp. 1097
    • Smith, L.D.1    Bungard, S.2    Danson, M.J.3    Hough, D.W.4
  • 27
    • 0027997111 scopus 로고
    • Determination of structure-antioxidart relationships of dihydrolipoic acid
    • Suzuki, Y. J., M. Tsuchiya, and L. Parker. 1994. Determination of structure-antioxidart relationships of dihydrolipoic acid. Methods Enzymol. 234:454-461.
    • (1994) Methods Enzymol. , vol.234 , pp. 454-461
    • Suzuki, Y.J.1    Tsuchiya, M.2    Parker, L.3
  • 29
    • 0026906511 scopus 로고
    • Dihydrolipoamide dehydrogenase from Haloferax volcanii: Gene cloning, complete primary sequence and comparison to other dihydrolipoamide dehydrogenases
    • Vettakkorumakankav, N. N., and K. J. Stevenson. 1992. Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning, complete primary sequence and comparison to other dihydrolipoamide dehydrogenases. Biochem. Cell Biol. 70:656-663.
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 656-663
    • Vettakkorumakankav, N.N.1    Stevenson, K.J.2
  • 30
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and J. Messing. 1991. New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100:189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 31
    • 0025767234 scopus 로고
    • Dihydrolipoic acid activates oligomycin-sensitive thiol groups and increases ATP synthesis in mitochondria
    • Zimmer, G., L. Mainka, and E. Kruger. 1991. Dihydrolipoic acid activates oligomycin-sensitive thiol groups and increases ATP synthesis in mitochondria. Arch. Biochem. Biophys. 288:609-613.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 609-613
    • Zimmer, G.1    Mainka, L.2    Kruger, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.